| Autor: |
Furutani, Shogo, Okuhara, Daiki, Hashimoto, Anju, Ihara, Makoto, Kai, Kenji, Hayashi, Hideo, Sattelle, David B., Matsuda, Kazuhiko |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; October 2017, Vol. 81 Issue: 10 p1861-1867, 7p |
| Abstrakt: |
Okaramines produced by Penicillium simplicissimumAK-40 activate l-glutamate-gated chloride channels (GluCls) and thus paralyze insects. However, the okaramine binding site on insect GluCls is poorly understood. Sequence alignment shows that the equivalent of residue Leucine319 of the okaramine B sensitive Bombyx mori(B. mori) GluCl is a phenylalanine in the okaramine B insensitive B. moriγ-aminobutyric acid-gated chloride channel of the same species. This residue is located in the third transmembrane (TM3) region, a location which in a nematode GluCl is close to the ivermectin binding site. The B. moriGluCl containing the L319F mutation retained its sensitivity to l-glutamate, but responses to ivermectin were reduced and those to okaramine B were completely blocked. |
| Databáze: |
Supplemental Index |
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